ArticleThe Biochemical journal2007
Human iron regulatory protein 2 is easily cleaved in its specific domain: consequences for the haem binding properties of the protein.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Using Biotinylated Iron-Responsive Element to Analyze the Activity of Iron Regulatory Proteins.International journal of molecular sciences · 2024Article
- Molecular Insight into Iron Homeostasis of Acute Myeloid Leukemia Blasts.International journal of molecular sciences · 2023Article
- Time-dependent effects of hypoxia on cell metabolism, signaling, and iron homeostasis in the hematopoietic progenitor model KG1a.FEBS open bio · 2023Article
- The Non-Canonical Iron-Responsive Element of IRE-tvcp12 Hairpin Structure at the 3'-UTR ofPathogens (Basel, Switzerland) · 2023Article
- FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster.Molecular cell · 2020Article
- ApoHRP-based assay to measure intracellular regulatory heme.Metallomics : integrated biometal science · 2015Article
- Heme sensor proteins.The Journal of biological chemistry · 2013Review
- Regulation of cellular iron metabolism.The Biochemical journal · 2011Review
- Unusual heme binding in the bacterial iron response regulator protein: spectral characterization of heme binding to the heme regulatory motif.Biochemistry · 2011Article
- Tumorigenic properties of iron regulatory protein 2 (IRP2) mediated by its specific 73-amino acids insert.PloS one · 2010Article
- Amyloid precursor protein and alpha synuclein translation, implications for iron and inflammation in neurodegenerative diseases.Biochimica et biophysica acta · 2009Review
- The functional duality of iron regulatory protein 1.Current opinion in structural biology · 2008Review
- Iron-dependent degradation of IRP2 requires its C-terminal region and IRP structural integrity.BMC molecular biology · 2008Article
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian IRPs (iron regulatory proteins), IRP1 and IRP2, are cytosolic RNA-binding proteins that post-transcriptionally control the mRNA of proteins involved in storage, transport, and utilization of iron. In iron-replete cells, IRP2 undergoes degradation by the ubiquitin/proteasome pathway. Binding of haem to a 73aa-Domain (73-amino-acid domain) that is unique in IRP2 has been previously proposed as the initial iron-sensing mechanism. It is shown here that recombinant IRP2 and the 73aa-Domain are sensitive to proteolysis at the same site. NMR results suggest that the isolated 73aa-Domain is not structured. Iron-independent cleavage of IRP2 within the 73aa-Domain also occurs in lung cancer (H1299) cells. Haem interacts with a cysteine residue only in truncated forms of the 73aa-Domain, as shown by a series of complementary physicochemical approaches, including NMR, EPR and UV-visible absorption spectroscopy. In contrast, the cofactor is not ligated by the same residue in the full-length peptide or intact IRP2, although non-specific interaction occurs between these molecular forms and haem. Therefore it is unlikely that the iron-dependent degradation of IRP2 is mediated by haem binding to the intact 73aa-Domain, since the sequence resembling an HRM (haem-regulatory motif) in the 73aa-Domain does not provide an axial ligand of the cofactor unless this domain is cleaved.
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